Paper Info
Title
Intrinsic Disorder In Protein Interactions: Insights From A Comprehensive Structural Analysis
Abstract
We perform a large-scale study of intrinsically disordered regions in proteins and protein complexes using a non-redundant set of hundreds of different protein complexes. In accordance with the conventional view that folding and binding are coupled, in many of our cases the disorder-to-order transition occurs upon complex formation and can be localized to binding interfaces. Moreover, analysis of disorder in protein complexes depicts a significant fraction of intrinsically disordered regions, with up to one third of all residues being disordered. We find that the disorder in homodimers, especially in symmetrical homodimers, is significantly higher than in heterodimers and offer an explanation for this interesting phenomenon. We argue that the mechanisms of regulation of binding specificity through disordered regions in complexes can be as common as for unbound monomeric proteins. The fascinating diversity of roles of disordered regions in various biological processes and protein oligomeric forms shown in our study may be a subject of future endeavors in this area.
Year
DOI
Venue
2009
10.1371/journal.pcbi.1000316
PLOS COMPUTATIONAL BIOLOGY
Keywords
Field
DocType
protein binding,structure analysis,biological process,computer simulation,proteins,binding sites,protein complex,amino acid sequence
Sequence alignment,Plasma protein binding,Protein structure prediction,Binding site,Protein–protein interaction,Biology,Intrinsically disordered proteins,Bioinformatics,Binding selectivity,Protein structure
Journal
Volume
Issue
ISSN
5
3
1553-734X
Citations 
PageRank 
References 
5
0.59
14
Authors
6
Name
Order
Citations
PageRank
Jessica H Fong117617.28
Benjamin A. Shoemaker2779244.03
Sergiy O. Garbuzynskiy39512.37
Michail Yu. Lobanov47910.18
Oxana V. Galzitskaya512520.15
Anna R. Panchenko6907252.52